1llf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:15, 16 August 2023) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1llf.gif|left|200px]]
 
-
{{Structure
+
==Cholesterol Esterase (Candida Cylindracea) Crystal Structure at 1.4A resolution==
-
|PDB= 1llf |SIZE=350|CAPTION= <scene name='initialview01'>1llf</scene>, resolution 1.4&Aring;
+
<StructureSection load='1llf' size='340' side='right'caption='[[1llf]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=F23:TRICOSANOIC+ACID'>F23</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
+
<table><tr><td colspan='2'>[[1llf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Limtongozyma_cylindracea Limtongozyma cylindracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LLF FirstGlance]. <br>
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F23:TRICOSANOIC+ACID'>F23</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1llf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1llf OCA], [https://pdbe.org/1llf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1llf RCSB], [https://www.ebi.ac.uk/pdbsum/1llf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1llf ProSAT]</span></td></tr>
-
|RELATEDENTRY=[[1cle|1CLE]]
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1llf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1llf OCA], [http://www.ebi.ac.uk/pdbsum/1llf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1llf RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/Q6S5M9_9ASCO Q6S5M9_9ASCO]
-
 
+
== Evolutionary Conservation ==
-
'''Cholesterol Esterase (Candida Cylindracea) Crystal Structure at 1.4A resolution'''
+
[[Image:Consurf_key_small.gif|200px|right]]
-
 
+
Check<jmol>
-
 
+
<jmolCheckbox>
-
==Overview==
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ll/1llf_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1llf ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
The three-dimensional structure of a Candida cylindracea cholesterol esterase (ChE) homodimer (534 x 2 amino acids) in complex with a ligand of proposed formula C(23)H(48)O(2) has been determined at 1.4 A resolution in space group P1 using synchrotron low-temperature data. The structure refined to R = 0.136 and R(free) = 0.169 and has revealed new stereochemical details in addition to those detected for the apo- and holo-forms at 1.9 and 2.0 A resolution, respectively [Ghosh et al. (1995), Structure, 3, 279-288]. The cholesterol esterase structure is a dimer with four spatially separated interfacial contact areas and two symmetry-related pairs of openings to an internal intradimer cavity. Hydrophobic active-site gorges in each subunit face each other across a central interfacial cavity. The ChE subunits have carbohydrate chains attached to their Asn314 and Asn351 residues, with two ordered N-acetyl-D-glucosoamine moieties visible at each site. The side chains of 14 residues have two alternative conformations with occupancy values of 0.5 +/- 0.2. For each subunit the electron density in the enzyme active-site gorge is well modeled by a C(23)-chain fatty acid.
The three-dimensional structure of a Candida cylindracea cholesterol esterase (ChE) homodimer (534 x 2 amino acids) in complex with a ligand of proposed formula C(23)H(48)O(2) has been determined at 1.4 A resolution in space group P1 using synchrotron low-temperature data. The structure refined to R = 0.136 and R(free) = 0.169 and has revealed new stereochemical details in addition to those detected for the apo- and holo-forms at 1.9 and 2.0 A resolution, respectively [Ghosh et al. (1995), Structure, 3, 279-288]. The cholesterol esterase structure is a dimer with four spatially separated interfacial contact areas and two symmetry-related pairs of openings to an internal intradimer cavity. Hydrophobic active-site gorges in each subunit face each other across a central interfacial cavity. The ChE subunits have carbohydrate chains attached to their Asn314 and Asn351 residues, with two ordered N-acetyl-D-glucosoamine moieties visible at each site. The side chains of 14 residues have two alternative conformations with occupancy values of 0.5 +/- 0.2. For each subunit the electron density in the enzyme active-site gorge is well modeled by a C(23)-chain fatty acid.
-
==About this Structure==
+
Three-dimensional structure of homodimeric cholesterol esterase-ligand complex at 1.4 A resolution.,Pletnev V, Addlagatta A, Wawrzak Z, Duax W Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):50-6. Epub 2002 Dec, 19. PMID:12499539<ref>PMID:12499539</ref>
-
1LLF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Candida_cylindracea Candida cylindracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLF OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Three-dimensional structure of homodimeric cholesterol esterase-ligand complex at 1.4 A resolution., Pletnev V, Addlagatta A, Wawrzak Z, Duax W, Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):50-6. Epub 2002 Dec, 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12499539 12499539]
+
</div>
-
[[Category: Candida cylindracea]]
+
<div class="pdbe-citations 1llf" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
-
[[Category: Triacylglycerol lipase]]
+
-
[[Category: Addlagatta, A.]]
+
-
[[Category: Duax, W.]]
+
-
[[Category: Pletnev, V.]]
+
-
[[Category: Wawrzak, Z.]]
+
-
[[Category: candida cylindracea cholesterol esterase]]
+
-
[[Category: crystal structure]]
+
-
[[Category: sterol ester acylhydrolase]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:04:16 2008''
+
==See Also==
 +
*[[Cholesterol esterase|Cholesterol esterase]]
 +
*[[Cholesterol esterase 3D structures|Cholesterol esterase 3D structures]]
 +
*[[Lipase 3D Structures|Lipase 3D Structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Limtongozyma cylindracea]]
 +
[[Category: Addlagatta A]]
 +
[[Category: Duax W]]
 +
[[Category: Pletnev V]]
 +
[[Category: Wawrzak Z]]

Current revision

Cholesterol Esterase (Candida Cylindracea) Crystal Structure at 1.4A resolution

PDB ID 1llf

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools